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Database: UniProt/TrEMBL
Entry: A0A0A2SEW7_9BACI
LinkDB: A0A0A2SEW7_9BACI
Original site: A0A0A2SEW7_9BACI 
ID   A0A0A2SEW7_9BACI        Unreviewed;       167 AA.
AC   A0A0A2SEW7;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   25-OCT-2017, entry version 19.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=NP92_12525 {ECO:0000313|EMBL:KGP59715.1};
OS   Anoxybacillus gonensis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX   NCBI_TaxID=198467 {ECO:0000313|EMBL:KGP59715.1, ECO:0000313|Proteomes:UP000030117};
RN   [1] {ECO:0000313|EMBL:KGP59715.1, ECO:0000313|Proteomes:UP000030117}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G2 {ECO:0000313|EMBL:KGP59715.1,
RC   ECO:0000313|Proteomes:UP000030117};
RA   Belduz A.O., Canakci S., Chan K.-G., Ee R., Mukminin Kahar U.,
RA   Suriaty Yaakop A., Goh K.M.;
RT   "Genome sequence of Anoxybacillus gonensis G2T isolated from Gonen hot
RT   spring in Turkey: a potential thermozymes producer.";
RL   Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|RuleBase:RU000393}.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {ECO:0000256|RuleBase:RU000393}.
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 copper ion per subunit.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 zinc ion per subunit.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000256|RuleBase:RU000393}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KGP59715.1}.
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DR   EMBL; JRZG01000019; KGP59715.1; -; Genomic_DNA.
DR   EnsemblBacteria; KGP59715; KGP59715; NP92_12525.
DR   KEGG; agn:AFK25_12520; -.
DR   KO; K04565; -.
DR   Proteomes; UP000030117; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR   Gene3D; 2.60.40.200; -; 1.
DR   InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR   InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR   InterPro; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   PANTHER; PTHR10003; PTHR10003; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   SUPFAM; SSF49329; SSF49329; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000030117};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       30    164       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   167 AA;  17938 MW;  43AC84C396FE6289 CRC64;
     MIICVVLFLL SGCMEEKVKN VDVNMINEDS DSIGTIKMSQ QPEGVKLDID LKGLPPGEHA
     IHIHDKGTCE PPTFQSAGEH FNPEGKEHGL LHPEGAHAGD LPNLIVKEDG TVKVQLMAPN
     VNLSEEKNGL FTKNGTSIVI HEGKDDGMSQ PAGNAGKRIA CGVIKKR
//
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